Laminin B (Domain IV);

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451     990 FWSLPASFRGDKVTSYGGELRFTVMQRPRPSSAPLHRQPLVVLQGNNIVLEHHASRD--PSPGQPSNFIVPFQEQAWQRP 1067
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQppPDPGQEQTYSVRLHEENWRDS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1172451    1068 DGQPATREHLLMALAGIDALLIQASYTQQPAESRLSGISMDVAVPENTGQdSAREVE 1124
Cdd:pfam00052   81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGP-PASWVE 136

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451  1770 IMVTVEEQRSQSVRPGADVTFICTAKSKSPAYTLVWTRlHNGKLPSRAMDFNGILTIRNVQPSDAGTYVCTGSNMFAMDQ 1849
Cdd:cd05754    1 IQVTVEEPRSQEVRPGADVSFICRAKSKSPAYTLVWTR-VNGTLPSRAMDFNGILTIRNVQLSDAGTYVCTGSNMLDTDE 79

                 ....*.
gi 1172451  1850 GTATLH 1855
Cdd:cd05754   80 ATATLY 85

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172451   421 GQTVTFTCVATGVPTPIINWRLNWGHIPAHPRVTMTSEGGRGTLIIRDVKEADQGAYTCEAMNSRGMVFGIPDGVLEL 498
Cdd:cd05743    1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGMVFGIPDGILTV 78

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451  3520 GAYFYDNGFLGLPGNSFSRSlpevPETIEFEVRTSTADGLLLWQGVvreaSRSKDFISLGLQDGHLVFSYQLGSGEARLV 3599
Cdd:cd00110    1 GVSFSGSSYVRLPTLPAPRT----RLSISFSFRTTSPNGLLLYAGS----QNGGDFLALELEDGRLVLRYDLGSGSLVLS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172451  3600 SGDPINDGEWHRITALREGQRGSIQVDGEDLVTGRSPGPNVAVNTKDIIYIGGAPDVATLTRGKFSSGITGCIKNLVLH 3678
Cdd:cd00110   73 SKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451       80 QMVYFRALVNFTRS----IEYSPQLEDASAKEFREVSEAVVEKLEPEYRKIPGDQIVSVVFIKELDGW-VFVELDVGSEG 154
Cdd:smart00200    1 PTQSFGVSLSVLSVegenLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEFRNGsVVVDLGLLFNE 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 1172451      155 NAD-GSQIQEVLHTVVSSGSIGPYVTSPWGFKFRRLGTVPQ 194
Cdd:smart00200   81 GVTnGQDVEEDLLQVIKQAAYSLKITNVNVVDVLDPDSADS 121

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451  2535 VQVEESELTLEAGHTATLHCSATGNPPPTIHWSKLRAPL---PWQHRIEGNTLVIPRVAQQDSGQYICNATNSAGHTEAT 2611
Cdd:cd20978    4 IQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLqgpMERATVEDGTLTIINVQPEDTGYYGCVATNEIGDIYTE 83

                 ....*
gi 1172451  2612 VVLHV 2616
Cdd:cd20978   84 TLLHV 88

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451  2726 TPQLETRNIGASVEFHCAVPNERGTHLRWLKEGGQLPPG--HSVQDGVLRIQNLDQNCQGTYVCQAHGPWGQAQATAQLI 2803
Cdd:cd05725    3 RPQNQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKGryEILDDHSLKIRKVTAGDMGSYTCVAENMVGKIEASATLT 82

                 .
gi 1172451  2804 V 2804
Cdd:cd05725   83 V 83

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451     1682 PSRSVVPQGGPHSLRCQVSGSPPHYFYWSREDGRPLPS----SAQQRHQGSELHFPSVQPSDAGVYICTCRNLIHTSNSR 1757
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAEsgrfSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                    ....*
gi 1172451     1758 AELLV 1762
Cdd:smart00410   81 TTLTV 85

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451     2058 SSSSRVAEGQTLDLNCVVPGHAHAQVTWHKRGGSLPT-------HHQTHGSRLRLYQVSSADSGEYVCSVLSSSGPLEAS 2130
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAesgrfsvSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                    ....*
gi 1172451     2131 VLVSI 2135
Cdd:smart00410   81 TTLTV 85

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451     1871 PPQLTVQPGQQAEFRCSATGNPTPMLEWIGGPSGQLPAKAQI------HNGILRLPAIEPSDQGQYLCRALSSAGQHVAR 1944
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFsvsrsgSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                    ....*
gi 1172451     1945 AMLQV 1949
Cdd:smart00410   81 TTLTV 85

Low-density lipoprotein receptor domain class A;

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1172451     283 SACGPQEASCHSGHCIPRDYLCDGQEDCRDGSDELGC 319
Cdd:pfam00057    1 STCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451     2253 SSSSHLTEGQTVDLKCVVPGQAHAQVTWHKRGSSLPA-------RHQTHGSLLRLYQLSPADSGEYVCQvAGSSHPEHEA 2325
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAesgrfsvSRSGSTSTLTISNVTPEDSGTYTCA-ATNSSGSASS 79

                    ....*.
gi 1172451     2326 SFKLTV 2331
Cdd:smart00410   80 GTTLTV 85

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172451    2828 EFECLALGDPKPQVTWSKVGGHLRPG----IVQSGTI--IRIAHVELADAGQYRCAATNAAGTTQSHVLLLV 2893
Cdd:pfam07679   19 RFTCTVTGTPDPEVSWFKDGQPLRSSdrfkVTYEGGTytLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1172451  1563 CECNGHSDL---CHPETGACsRCQHNTAGEFCELCATGYYGDATAgtPEDCQ 1611
Cdd:cd00055    2 CDCNGHGSLsgqCDPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 1172451   199 CTETEFACHSyNECVALEYRCDRRPDCRDMSDELNC 234
Cdd:cd00112    1 CPPNEFRCAN-GRCIPSSWVCDGEDDCGDGSDEENC 35

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 1172451  3462 NPCQLHEPCLNGGTCR----GARCLCLPGFSGPRCQ 3493
Cdd:cd00054    3 DECASGNPCQNGGTCVntvgSYRCSCPPGYTGRNCE 38

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1172451   813 PCPCPYIDASrrfSDTCFLDTdGQatCDaCAPGYTGRRCESCAPGYEGNPIQPGGkCR 870
Cdd:cd00055    1 PCDCNGHGSL---SGQCDPGT-GQ--CE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1172451  1612 PCACPLTNPENMfsrTCESlgaGGYRCTaCEPGYTGQYCEQCAPGYEGDPNvQGGRCQ 1669
Cdd:cd00055    1 PCDCNGHGSLSG---QCDP---GTGQCE-CKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.

                           10        20        30
                   ....*....|....*....|....*....|.
gi 1172451    3425 CERQPCRNGATCMPAGEyEFQCLCQDGFKGD 3455
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPG-GYTCICPEGYTGK 30

Laminin B (Domain IV);

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451     990 FWSLPASFRGDKVTSYGGELRFTVMQRPRPSSAPLHRQPLVVLQGNNIVLEHHASRD--PSPGQPSNFIVPFQEQAWQRP 1067
Cdd:pfam00052    1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQppPDPGQEQTYSVRLHEENWRDS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1172451    1068 DGQPATREHLLMALAGIDALLIQASYTQQPAESRLSGISMDVAVPENTGQdSAREVE 1124
Cdd:pfam00052   81 DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGP-PASWVE 136

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451  1770 IMVTVEEQRSQSVRPGADVTFICTAKSKSPAYTLVWTRlHNGKLPSRAMDFNGILTIRNVQPSDAGTYVCTGSNMFAMDQ 1849
Cdd:cd05754    1 IQVTVEEPRSQEVRPGADVSFICRAKSKSPAYTLVWTR-VNGTLPSRAMDFNGILTIRNVQLSDAGTYVCTGSNMLDTDE 79

                 ....*.
gi 1172451  1850 GTATLH 1855
Cdd:cd05754   80 ATATLY 85

Laminin B domain;

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451     1393 ESFYWQLPEIYQGDKVAAYGGKLRYTLSYTAGPQGSPLLDPDIQITGNNIMLVASQPALQGPERRSY-EIIFREEFWRRP 1471
Cdd:smart00281    3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGTHVSAPDVILEGNGLRISHPAEGPPLPDELTTvEVRFREENWQYY 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 1172451     1472 DGQPATREHLLMALADLDELLVRATFSSVPRAASISAVSLEGAQP 1516
Cdd:smart00281   83 GGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172451   421 GQTVTFTCVATGVPTPIINWRLNWGHIPAHPRVTMTSEGGRGTLIIRDVKEADQGAYTCEAMNSRGMVFGIPDGVLEL 498
Cdd:cd05743    1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGMVFGIPDGILTV 78

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451  3251 GAGSYLALPALTNTHHELRLDVEFKPLEPNGILLFSGGKSGPveDFVSLAMVGGHLEFRYELGSGLAVLRSHEPLALGRW 3330
Cdd:cd00110    5 SGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGG--DFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQW 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451  3331 HRVSAERLNKDGSLRVDGGRPVLRSSPGKSQGLNLHTLLYLGGVePSVQLSPATNMSAHFHGCVGEVSVN 3400
Cdd:cd00110   83 HSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGL-PEDLKSPGLPVSPGFVGCIRDLKVN 151

Laminin G domain;

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451     3269 RLDVEFKPLEPNGILLFSGGKSGPveDFVSLAMVGGHLEFRYELGSGLAVLRS-HEPLALGRWHRVSAERLNKDGSLRVD 3347
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGG--DYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVD 78

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1172451     3348 GGRPVLRSSPGKSQGLNLHTLLYLGGVePSVQLSPATNMSAHFHGCVGEVSVNGK 3402
Cdd:smart00282   79 GGNRVSGESPGGLTILNLDGPLYLGGL-PEDLKLPPLPVTPGFRGCIRNLKVNGK 132

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451  2986 YFTQTpySFLPLPTIKDAYRKFEIKITFRPDSADGMLLYNGQKRsptnlanrQPDFISFGLVGGRPEFRFDAGSGMATIR 3065
Cdd:cd00110    3 SFSGS--SYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQN--------GGDFLALELEDGRLVLRYDLGSGSLVLS 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172451  3066 HPTPLALGQFHTVTLLRSLTQGSLIVGNLAPVNGTSQGKFQGLDLNEELYLGGYPDYGAIPKAGLSSGFVGCVRELRI 3143
Cdd:cd00110   73 SKTPLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150

Laminin G domain;

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451     3008 EIKITFRPDSADGMLLYNGQKRsptnlanrQPDFISFGLVGGRPEFRFDAGSGMATIRH-PTPLALGQFHTVTLLRSLTQ 3086
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKG--------GGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRS 72

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451     3087 GSLIVGNLAPVNGTSQGKFQGLDLNEELYLGGYPDYGAIPKAGLSSGFVGCVRELRIQGE 3146
Cdd:smart00282   73 VTLSVDGGNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132

Laminin G domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172451    3013 FRPDSADGMLLYNGQkrsptnlaNRQPDFISFGLVGGRPEFRFDAGSGMATIRHPTPLALGQFHTVTLLRSLTQGSLIVG 3092
Cdd:pfam00054    1 FRTTEPSGLLLYNGT--------QTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVD 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1172451    3093 NLAPVNGTSQ-GKFQGLDLNEELYLGGYPDYGAIPKAG-LSSGFVGCVRELRIQGEEI 3148
Cdd:pfam00054   73 GEARPTGESPlGATTDLDVDGPLYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNGKPL 130

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1172451      413 QQSIQASRGQTVTFTCVATGVPTPIINWRLNWGHIPAHP-RVTMTSEGGRGTLIIRDVKEADQGAYTCEAMNSRGMVFG 490
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESgRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASS 79

Immunoglobulin I-set domain;